Endosomal endothelin-converting enzyme-1: a regulator of beta-arrestin-dependent ERK signaling.

@article{Cottrell2009EndosomalEE,
  title={Endosomal endothelin-converting enzyme-1: a regulator of beta-arrestin-dependent ERK signaling.},
  author={Graeme S Cottrell and Benjamin E Padilla and Silvia Amadesi and Daniel P Poole and Jane E. Murphy and M. Hardt and Dirk Roosterman and Martin S Steinhoff and Nigel W Bunnett},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 33},
  pages={
          22411-25
        }
}
Neuropeptide signaling at the cell surface is regulated by metalloendopeptidases, which degrade peptides in the extracellular fluid, and beta-arrestins, which interact with G protein-coupled receptors (GPCRs) to mediate desensitization. beta-Arrestins also recruit GPCRs and mitogen-activated protein kinases to endosomes to allow internalized receptors to continue signaling, but the mechanisms regulating endosomal signaling are unknown. We report that endothelin-converting enzyme-1 (ECE-1… CONTINUE READING
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